Monoclonal antibodies have become important pharmaceuticals, largely due to the high affinities and selectivity that are possible to achieve with monoclonals. Since the first development of monoclonal antibodies in the 1970s, the use of monoclonal antibodies specific to disease targets of interest has provided new therapeutic options for treatment of various diseases, including but not limited to cancer and autoimmune diseases.
Although methods for producing and using monoclonal antibodies have improved over time, the methods used to identify new monoclonal antibodies are not robust and reliable. For example, immunization of human Ig transgenic mice does not guarantee a yield of high affinity antibodies. Further, hybridoma generation and screening is tedious and time consuming. Additionally, although antibody phage display offers many advantages over the use of transgenic mice, the screening effort is daunting. In these methods, the library size requirement and the necessity of pairing heavy and light chain genes in their original configuration is time intensive and not guaranteed. Thus, easy methods that facilitate reliable isolation and identification of antibodies are needed.